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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Unc-51 like kinase 2

This gene encodes a protein that is similar to a serine/threonine kinase in C. elegans which is involved in axonal elongation. The structure of this protein is similar to the C. elegans protein in that both proteins have an N-terminal kinase domain, a central proline/serine rich (PS) domain, and a C-terminal (C) domain. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Dec 2008] (from NCBI)
Top mentioned proteins: Atg1, CC-1, Atg5, LC3, mTORC1
Papers on ULK2
Atg101: not just an accessory subunit in the autophagy-initiation complex.
Mizushima et al., In Cell Struct Funct, Feb 2016
UNASSIGNED: The Saccharomyces cerevisiae autophagy-initiation complex, Atg1 kinase complex, consists of Atg1, Atg13, Atg17, Atg29, and Atg31, while the corresponding complex in most other eukaryotes, including mammals, is composed of ULK1 (or ULK2), Atg13, FIP200 (also known as RB1CC1), and Atg101.
Atg13 is essential for autophagy and cardiac development in mice.
Mizushima et al., Tokyo, Japan. In Mol Cell Biol, Jan 2016
Among them, the ULK1 complex, which is composed of ULK1 (or ULK2), FIP200, Atg13, and Atg101, acts at an initial step.
Alteration of Upstream Autophagy-Related Proteins (ULK1, ULK2, Beclin1, VPS34 and AMBRA1) in Lewy Body Disease.
Wakabayashi et al., Hirosaki, Japan. In Brain Pathol, Sep 2015
We performed immunostaining and Western blot analysis using a cellular model of PD and human brain samples to investigate the involvement of upstream autophagosomal proteins (ULK1, ULK2, Beclin1, VPS34 and AMBRA1), which initiate autophagy and form autophagosomes.
Pharmacological inhibition of ULK1 kinase blocks mammalian target of rapamycin (mTOR)-dependent autophagy.
Ganley et al., London, United Kingdom. In J Biol Chem, Jun 2015
ULK1, a serine/threonine protein kinase, is essential for the initial stages of autophagy, and here we report that two compounds, MRT67307 and MRT68921, potently inhibit ULK1 and ULK2 in vitro and block autophagy in cells.
Involvement of fish signal transducer and activator of transcription 3 (STAT3) in nodavirus infection induced cell death.
Qin et al., Guangzhou, China. In Fish Shellfish Immunol, Mar 2015
Further studies indicated that Ec-STAT3 inhibition significantly increased the transcript level of autophagy related genes, including UNC-51-like kinase 2 (ULK2) and microtubule-associated protein 1 light chain 3-II (LC3-II) induced by RGNNV infection.
ULK2 Ser 1027 Phosphorylation by PKA Regulates Its Nuclear Localization Occurring through Karyopherin Beta 2 Recognition of a PY-NLS Motif.
Kang et al., Ch'ŏngju, South Korea. In Plos One, 2014
Uncoordinated 51-like kinase 2 (ULK2), a member of the serine/threonine kinase family, plays an essential role in the regulation of autophagy in mammalian cells.
Differentially expressed genes in metastatic advanced Egyptian bladder cancer.
Abu-Taleb et al., Cairo, Egypt. In Asian Pac J Cancer Prev, 2014
RESULTS: Five hundred and sixteen genes were differentially expressed of which SOS1, HDAC2, PLXNC1, GTSE1, ULK2, IRS2, ABCA12, TOP3A, HES1, and SRP68 genes were involved in 33 different pathways.
Methylation silencing of ULK2, an autophagy gene, is essential for astrocyte transformation and tumor growth.
Somasundaram et al., Bengaluru, India. In J Biol Chem, 2014
One of the hypermethylated genes in GBM, ULK2, an upstream autophagy inducer, was found to be down-regulated in GBM.
Autophagy suppression by appendicitis and appendectomy protects against colitis.
Grimm et al., Sydney, Australia. In Inflamm Bowel Dis, 2014
RESULTS: Out of 28 key autophagy-related genes investigated (VPS15, VPS34, FIP200, ATG03, ATG04A, ATG04B, ATG05, ATG07, ATG10, ATG12, ATG13b, ATG14, ATG16L1, BECN1, GABARAPL1, IRGM1, IRGM2, LAMP2, LC3A, LC3B, RAB7A, UVRAG, NOD2, XBP1, LRRK2, ULK1, ULK2, PTPN2), 7 have genetic associations with inflammatory bowel diseases (ATG16L1, IRGM1, NOD2, XBP1, LRRK2, ULK1, PTPN2).
Analysis of a lung defect in autophagy-deficient mouse strains.
Lindsten et al., New York City, United States. In Autophagy, 2014
We created mice deficient for both Ulk1 and Ulk2 and found that the mice die within 24 h of birth.
Distinct functions of Ulk1 and Ulk2 in the regulation of lipid metabolism in adipocytes.
Kim et al., Minneapolis, United States. In Autophagy, 2013
In this study, we established autophagy defective-differentiated 3T3-L1 adipocytes, and investigated the roles of Ulk1 and its close homolog Ulk2 in lipid and glucose metabolism using the established adipocytes.
Autophagy and lysosomal related protein expression patterns in human glioblastoma.
Koukourakis et al., Alexandroúpolis, Greece. In Cancer Biol Ther, 2013
We investigated the patterns of expression of autophagy related proteins (LC3A, LC3B, p62, Beclin 1, ULK1 and ULK2) in a series of patients treated with post-operative radiotherapy.
Kctd12 and Ulk2 partner to regulate dendritogenesis and behavior in the habenular nuclei.
Gamse et al., Nashville, United States. In Plos One, 2013
The kinase Ulk2 positively regulates dendritogenesis on habenular neurons, and in turn is negatively regulated by the cytoplasmic protein Kctd12.
Upregulation of human autophagy-initiation kinase ULK1 by tumor suppressor p53 contributes to DNA-damage-induced cell death.
Wang et al., Dallas, United States. In Cell Death Differ, 2011
In response to DNA damage, ULK1 and ULK2 are upregulated by p53. The upregulation of ULK1 (ULK2)/ATG13 complex by p53 is necessary for the sustained autophagy activity induced by DNA damage.
Ammonia-induced autophagy is independent of ULK1/ULK2 kinases.
Thompson et al., Philadelphia, United States. In Proc Natl Acad Sci U S A, 2011
the autophagy response to the enhanced amino acid catabolism induced by deprivation of glucose or direct exposure to ammonia does not require ULK1 and/or ULK2
The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the regulation of autophagy.
Tournier et al., Manchester, United Kingdom. In Autophagy, 2011
ULK1 and ULK2 are functionally redundant protein kinases required to mediate autophagy under nutrient-deprived conditions in fibroblasts.
Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy.
Shaw et al., Los Angeles, United States. In Science, 2011
In a screen for conserved substrates of AMPK, we identified ULK1 and ULK2, mammalian orthologs of the yeast protein kinase Atg1, which is required for autophagy.
The role of the Atg1/ULK1 complex in autophagy regulation.
Mizushima, Tokyo, Japan. In Curr Opin Cell Biol, 2010
Recent studies of mammalian Atg1 homologs (ULK1 and ULK2) have identified several novel interacting proteins, FIP200, mAtg13, and Atg101.
ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery.
Kim et al., Minneapolis, United States. In Mol Biol Cell, 2009
The ULK-Atg13-FIP200 complexes are direct targets of mTOR and important regulators of autophagy in response to mTOR signaling.
Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism.
Tooze et al., London, United Kingdom. In Mol Cell Biol, 2009
The functions of ULK1 and ULK2 are controlled by autophosphorylation and conformational changes involving exposure of the C-terminal domain and interaction with the putative human homologue of Atg13.
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